Format

Send to

Choose Destination
See comment in PubMed Commons below
Plant Physiol Biochem. 2004 May;42(5):355-65.

The eight-cysteine motif, a versatile structure in plant proteins.

Author information

  • 1Laboratori de Genètica Molecular i Vegetal, Consorci CSIC-IRTA, Jordi Girona 18-26, 08034 Barcelona, Spain. mjegmp@ibmb.csic.es

Abstract

A number of protein sequences deduced from the molecular analysis of plant cDNA or genomic libraries can be grouped in relation to a defined number of cysteine residues located in distinct positions of their sequences. This is the case for a group of around 500 polypeptides from different species that contain a small domain (less than 100 amino acids residues) displaying a pattern of eight-cysteines in a specific order. The plant sequences containing this motif belong to proteins having different functions, ranging from storage, protection, enzyme inhibition and lipid transfer, to cell wall structure. The eight-cysteine motif (8CM) appears to be a structural scaffold of conserved helical regions connected by variable loops, as observed by three-dimensional structure analysis. It is proposed that the cysteine residues would form a network of disulfide bridges necessary, for the maintenance of the tertiary structure of the molecule together with the central helical core, while the variable loops would provide the sequences required for the specific functions of the proteins.

Copyright 2004 Elsevier SAS

[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Write to the Help Desk